Evidence map›Paper›PMID 26741367›Full record

ArticlePloS one2016

Comparing Residue Clusters from Thermophilic and Mesophilic Enzymes Reveals Adaptive Mechanisms.

Deanne W Sammond, Noah Kastelowitz, Michael E Himmel, Hang Yin, Michael F Crowley, Yannick J Bomble

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 30 citations in OpenAlex.

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  12. Improving the thermal stability of cellobiohydrolase Cel7A fromThe Journal of biological chemistry · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Deanne W SammondBiosciences Center, National Renewable Energy Laboratory, Golden, Colorado, 80401, United States of America.
Noah KastelowitzDepartment of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado, Boulder, Colorado, 80309, United States of America.
Michael E HimmelBiosciences Center, National Renewable Energy Laboratory, Golden, Colorado, 80401, United States of America.
Hang YinDepartment of Chemistry & Biochemistry and the BioFrontiers Institute, University of Colorado, Boulder, Colorado, 80309, United States of America.
Michael F CrowleyBiosciences Center, National Renewable Energy Laboratory, Golden, Colorado, 80401, United States of America.
Yannick J BombleBiosciences Center, National Renewable Energy Laboratory, Golden, Colorado, 80401, United States of America.
National Renewable Energy Laboratory · USUniversity of Colorado Boulder · US

Funding

Medical Scientist Training ProgramT32GM008497 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI WILSON, CARA C. · 1993 to 2022
$15.2M
Dissecting Cell Signaling Mediated by Protein-Protein Interactions in MembranesR01GM103843 · NIGMS · UNIVERSITY OF COLORADO · PI YIN, HANG HUBERT · 2013 to 2016
$1.3M
Microvesicles and exosomes as a cancer biomarker detected with designed peptidesF30CA180249 · NCI · UNIVERSITY OF COLORADO · PI KASTELOWITZ-LIEBERMAN, NOAH · 2013 to 2017
$195k
NCI NIH HHS F30 CA180249NCI NIH HHS F30CA180249NIGMS NIH HHS R01 GM103843NIGMS NIH HHS R01GM103843NIGMS NIH HHS T32 GM008497
6 · The paper itself

Abstract

Understanding how proteins adapt to function at high temperatures is important for deciphering the energetics that dictate protein stability and folding. While multiple principles important for thermostability have been identified, we lack a unified understanding of how internal protein structural and chemical environment determine qualitative or quantitative impact of evolutionary mutations. In this work we compare equivalent clusters of spatially neighboring residues between paired thermophilic and mesophilic homologues to evaluate adaptations under the selective pressure of high temperature. We find the residue clusters in thermophilic enzymes generally display improved atomic packing compared to mesophilic enzymes, in agreement with previous research. Unlike residue clusters from mesophilic enzymes, however, thermophilic residue clusters do not have significant cavities. In addition, anchor residues found in many clusters are highly conserved with respect to atomic packing between both thermophilic and mesophilic enzymes. Thus the improvements in atomic packing observed in thermophilic homologues are not derived from these anchor residues but from neighboring positions, which may serve to expand optimized protein core regions.

Indexed as

Amino AcidsAmino Acid SequenceAminopeptidasesArchaeaArchaeal ProteinsBacteriaBacterial ProteinsCluster AnalysisFungal ProteinsFungiHot TemperatureL-Lactate DehydrogenaseMalate DehydrogenaseModels, MolecularMolecular Sequence DataProtein FoldingAmino AcidsAminopeptidasesArchaeal ProteinsBacterial ProteinsFungal ProteinsL-Lactate DehydrogenaseMalate Dehydrogenase

Identifiers

PMID26741367
PMCPMC4704809
OpenAlexW2224693933

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.